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Literature summary for 5.1.2.2 extracted from

  • Landro, J.A.; Kallarakal, A.T.; Ransom, S.C.; Gerlt, J.A.; Kozarich, J.W.; Neidhart, D.J.; Kenyon, G.L.
    Mechanism of the reaction catalyzed by mandelate racemase. 3. Asymmetry in reactions catalyzed by the H297N mutant (1991), Biochemistry, 30, 9274-9281.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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Pseudomonas putida

Protein Variants

Protein Variants Comment Organism
H297N H297N has no detectable mandelate racemase activity. However, H297N catalyzes the stereospecific elimination of Br- from racemic p-(bromomethyl)mandelate to give p-(methyl)benzoylformate in 45% yield at a rate equal to that measured for wild type enzyme Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
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mutant gene H297N overexpressed in Pseudomonas aeruginosa
-

Reaction

Reaction Comment Organism Reaction ID
(S)-mandelate = (R)-mandelate reaction proceeds via a two-base mechanism in which Lys166 abstracts the alpha-proton from (S)-mandelate and His297 abstracts the alpha-proton from (R)-mandelate Pseudomonas putida
(S)-mandelate = (R)-mandelate the enzyme contains two distinct general acid/base catalysts: Lys166 which abstracts the alpha-proton from (S)-mandelate, and His297, which abstracts the alpha-proton from (R)-mandelate Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-mandelate
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Pseudomonas putida L-mandelate
-
?
p-(bromomethyl)mandelate
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Pseudomonas putida p-(methyl)benzoylformate + Br-
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information dependence of turnover number on pH Pseudomonas putida